메뉴 건너뛰기




Volumn 5, Issue , 2014, Pages

Emi2 mediates meiotic MII arrest by competitively inhibiting the binding of Ube2S to the APC/C

Author keywords

[No Author keywords available]

Indexed keywords

ANAPHASE PROMOTING COMPLEX; ANAPHASE PROMOTING COMPLEX SUBUNIT 10; APC PROTEIN; CYCLIN B; EMI2 PROTEIN; MEMBRANE PROTEIN; UBIQUITIN CONJUGATING ENZYME; UBIQUITIN CONJUGATING ENZYME E2; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG; F BOX PROTEIN; PROTEIN BINDING; XENOPUS PROTEIN;

EID: 84899634668     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms4667     Document Type: Article
Times cited : (35)

References (50)
  • 1
    • 0015076873 scopus 로고
    • Cytoplasmic control of nuclear behavior during meiotic maturation of frog oocytes
    • Masui, Y. & Markert, C. L. Cytoplasmic control of nuclear behavior during meiotic maturation of frog oocytes. J. Exp. Zool. 177, 129-145 (1971).
    • (1971) J. Exp. Zool , vol.177 , pp. 129-145
    • Masui, Y.1    Markert, C.L.2
  • 2
    • 0030046306 scopus 로고    scopus 로고
    • Meiotic metaphase arrest in animal oocytes: Its mechanisms and biological significance
    • DOI 10.1016/0962-8924(96)81034-8
    • Sagata, N. Meiotic metaphase arrest in animal oocytes: its mechanisms and biological significance. Trends Cell. Biol. 6, 22-28 (1996). (Pubitemid 26016557)
    • (1996) Trends in Cell Biology , vol.6 , Issue.1 , pp. 22-28
    • Sagata, N.1
  • 3
    • 33747589184 scopus 로고    scopus 로고
    • The anaphase promoting complex/cyclosome: A machine designed to destroy
    • Peters, J. M. The anaphase promoting complex/cyclosome: a machine designed to destroy. Nat. Rev. Mol. Cell Biol. 7, 644-656 (2006).
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 644-656
    • Peters, J.M.1
  • 4
    • 0037444220 scopus 로고    scopus 로고
    • Under arrest: Cytostatic factor (CSF)-mediated metaphase arrest in vertebrate eggs
    • DOI 10.1101/gad.1071303
    • Tunquist, B. J. & Maller, J. L. Under arrest: cytostatic factor (CSF)-mediated metaphase arrest in vertebrate eggs. Genes Dev. 17, 683-710 (2003). (Pubitemid 36359187)
    • (2003) Genes and Development , vol.17 , Issue.6 , pp. 683-710
    • Tunquist, B.J.1    Maller, J.L.2
  • 8
    • 34247600518 scopus 로고    scopus 로고
    • A direct link of the Mos-MAPK pathway to Erp1/Emi2 in meiotic arrest of Xenopus laevis eggs
    • DOI 10.1038/nature05688, PII NATURE05688
    • Inoue, D., Ohe, M., Kanemori, Y., Nobui, T. & Sagata, N. A direct link of the Mos-MAPK pathway to Erp1/Emi2 in meiotic arrest of Xenopus laevis eggs. Nature 446, 1100-1104 (2007). (Pubitemid 46676048)
    • (2007) Nature , vol.446 , Issue.7139 , pp. 1100-1104
    • Inoue, D.1    Ohe, M.2    Kanemori, Y.3    Nobui, T.4    Sagata, N.5
  • 9
    • 34247586577 scopus 로고    scopus 로고
    • Phosphorylation of Erp1 by p90rsk is required for cytostatic factor arrest in Xenopus laevis eggs
    • DOI 10.1038/nature05696, PII NATURE05696
    • Nishiyama, T., Ohsumi, K. & Kishimoto, T. Phosphorylation of Erp1 by p90rsk is required for cytostatic factor arrest in Xenopus laevis eggs. Nature 446, 1096-1099 (2007). (Pubitemid 46676049)
    • (2007) Nature , vol.446 , Issue.7139 , pp. 1096-1099
    • Nishiyama, T.1    Ohsumi, K.2    Kishimoto, T.3
  • 10
    • 33845958134 scopus 로고    scopus 로고
    • The anaphase-promoting complex/cyclosome inhibitor Emi2 Is essential for meiotic but not mitotic cell cycles
    • DOI 10.1074/jbc.M606607200
    • Liu, J., Grimison, B., Lewellyn, A. L. & Maller, J. L. The anaphase-promoting complex/cyclosome inhibitor Emi2 is essential for meiotic but not mitotic cell cycles. J. Biol. Chem. 281, 34736-34741 (2006). (Pubitemid 46036513)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.46 , pp. 34736-34741
    • Liu, J.1    Grimison, B.2    Lewellyn, A.L.3    Maller, J.L.4
  • 11
    • 33748565597 scopus 로고    scopus 로고
    • Mouse Emi2 is required to enter meiosis II by reestablishing cyclin B1 during interkinesis
    • DOI 10.1083/jcb.200604140
    • Madgwick, S., Hansen, D. V., Levasseur, M., Jackson, P. K. & Jones, K. T. Mouse Emi2 is required to enter meiosis II by reestablishing cyclin B1 during interkinesis. J. Cell Biol. 174, 791-801 (2006). (Pubitemid 44373729)
    • (2006) Journal of Cell Biology , vol.174 , Issue.6 , pp. 791-801
    • Madgwick, S.1    Hansen, D.V.2    Levasseur, M.3    Jackson, P.K.4    Jones, K.T.5
  • 12
    • 0024313534 scopus 로고
    • The c-mos proto-oncogene product is a cytostatic factor responsible for meiotic arrest in vertebrate eggs
    • DOI 10.1038/342512a0
    • Sagata, N., Watanabe, N., Vande Woude, G. F. & Ikawa, Y. The c-mos protooncogene product is a cytostatic factor responsible for meiotic arrest in vertebrate eggs. Nature 342, 512-518 (1989). (Pubitemid 20005815)
    • (1989) Nature , vol.342 , Issue.6249 , pp. 512-518
    • Sagata, N.1    Watanabe, N.2    Vande Woude, G.F.3    Ikawa, Y.4
  • 13
    • 33646794376 scopus 로고    scopus 로고
    • Cytostatic factor: An activity that puts the cell cycle on hold
    • Schmidt, A., Rauh, N. R., Nigg, E. A. & Mayer, T. U. Cytostatic factor: an activity that puts the cell cycle on hold. J. Cell Sci. 119, 1213-1218 (2006).
    • (2006) J. Cell Sci , vol.119 , pp. 1213-1218
    • Schmidt, A.1    Rauh, N.R.2    Nigg, E.A.3    Mayer, T.U.4
  • 14
    • 31444440363 scopus 로고    scopus 로고
    • CaMKII and Polo-like kinase 1 sequentially phosphorylate the cytostatic factor Emi2/XErp1 to trigger its destruction and meiotic exit
    • DOI 10.1073/pnas.0509549102
    • Hansen, D. V., Tung, J. J. & Jackson, P. K. CaMKII and polo-like kinase 1 sequentially phosphorylate the cytostatic factor Emi2/XErp1 to trigger its destruction and meiotic exit. Proc. Natl Acad. Sci. USA 103, 608-613 (2006). (Pubitemid 43153073)
    • (2006) Proceedings of the National Academy of Sciences of the United States of America , vol.103 , Issue.3 , pp. 608-613
    • Hansen, D.V.1    Tung, J.J.2    Jackson, P.K.3
  • 15
    • 27144516795 scopus 로고    scopus 로고
    • Calcium triggers exit from meiosis II by targeting the APC/C inhibitor XErp1 for degradation
    • DOI 10.1038/nature04093, PII N04093
    • Rauh, N. R., Schmidt, A., Bormann, J., Nigg, E. A. & Mayer, T. U. Calcium triggers exit from meiosis II by targeting the APC/C inhibitor XErp1 for degradation. Nature 437, 1048-1052 (2005). (Pubitemid 41486988)
    • (2005) Nature , vol.437 , Issue.7061 , pp. 1048-1052
    • Rauh, N.R.1    Schmidt, A.2    Bormann, J.3    Nigg, E.A.4    Mayer, T.U.5
  • 17
    • 77955115812 scopus 로고    scopus 로고
    • Emi2-mediated inhibition of E2-substrate ubiquitin transfer by the APC/C through a D-Box-independent mechanism
    • Tang, W. et al. Emi2-mediated inhibition of E2-substrate ubiquitin transfer by the APC/C through a D-Box-independent mechanism. Mol. Biol. Cell 21, 2589-2597 (2010).
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2589-2597
    • Tang, W.1
  • 18
    • 77949446825 scopus 로고    scopus 로고
    • Emi2 inhibition of the anaphase-promoting complex/cyclosome absolutely requires Emi2 binding via the C-terminal RL tail
    • Ohe, M. et al. Emi2 inhibition of the anaphase-promoting complex/cyclosome absolutely requires Emi2 binding via the C-terminal RL tail. Mol. Biol. Cell 21, 905-913 (2010).
    • (2010) Mol. Biol. Cell , vol.21 , pp. 905-913
    • Ohe, M.1
  • 19
    • 80052749932 scopus 로고    scopus 로고
    • Dynamic regulation of Emi2 by Emi2-bound Cdk1/Plk1/CK1 and PP2A-B56 in meiotic arrest of Xenopus eggs
    • Isoda, M. et al. Dynamic regulation of Emi2 by Emi2-bound Cdk1/Plk1/CK1 and PP2A-B56 in meiotic arrest of Xenopus eggs. Dev. Cell 21, 506-519 (2011).
    • (2011) Dev. Cell , vol.21 , pp. 506-519
    • Isoda, M.1
  • 21
    • 81055139468 scopus 로고    scopus 로고
    • Structural insights into anaphase-promoting complex function and mechanism
    • Barford, D. Structural insights into anaphase-promoting complex function and mechanism. Philos. Trans. R. Soc. Lond. B Biol. Sci. 366, 3605-3624 (2011).
    • (2011) Philos. Trans. R. Soc. Lond. B Biol. Sci , vol.366 , pp. 3605-3624
    • Barford, D.1
  • 22
    • 79959555511 scopus 로고    scopus 로고
    • Cubism and the cell cycle: The many faces of the APC/C
    • Pines, J. Cubism and the cell cycle: the many faces of the APC/C. Nat. Rev. Mol. Cell Biol. 12, 427-438 (2011).
    • (2011) Nat. Rev. Mol. Cell Biol , vol.12 , pp. 427-438
    • Pines, J.1
  • 23
    • 79959908728 scopus 로고    scopus 로고
    • Emerging roles for Lys11-linked polyubiquitin in cellular regulation
    • Bremm, A. & Komander, D. Emerging roles for Lys11-linked polyubiquitin in cellular regulation. Trends Biochem. Sci. 36, 355-363 (2011).
    • (2011) Trends Biochem. Sci , vol.36 , pp. 355-363
    • Bremm, A.1    Komander, D.2
  • 24
    • 43049162227 scopus 로고    scopus 로고
    • Mechanism of Ubiquitin-Chain Formation by the Human Anaphase-Promoting Complex
    • DOI 10.1016/j.cell.2008.04.012, PII S0092867408005035
    • Jin, L., Williamson, A., Banerjee, S., Philipp, I. & Rape, M. Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex. Cell 133, 653-665 (2008). (Pubitemid 351636306)
    • (2008) Cell , vol.133 , Issue.4 , pp. 653-665
    • Jin, L.1    Williamson, A.2    Banerjee, S.3    Philipp, I.4    Rape, M.5
  • 25
    • 49349089823 scopus 로고    scopus 로고
    • The unique N terminus of the UbcH10 E2 enzyme controls the threshold for APC activation and enhances checkpoint regulation of the APC
    • Summers, M. K., Pan, B., Mukhyala, K. & Jackson, P. K. The unique N terminus of the UbcH10 E2 enzyme controls the threshold for APC activation and enhances checkpoint regulation of the APC. Mol. Cell 31, 544-556 (2008).
    • (2008) Mol. Cell , vol.31 , pp. 544-556
    • Summers, M.K.1    Pan, B.2    Mukhyala, K.3    Jackson, P.K.4
  • 26
    • 70449529843 scopus 로고    scopus 로고
    • UBE2S elongates ubiquitin chains on APC/C substrates to promote mitotic exit
    • Garnett, M. J. et al. UBE2S elongates ubiquitin chains on APC/C substrates to promote mitotic exit. Nat. Cell Biol. 11, 1363-1369 (2009).
    • (2009) Nat. Cell Biol , vol.11 , pp. 1363-1369
    • Garnett, M.J.1
  • 27
    • 70849116420 scopus 로고    scopus 로고
    • Identification of a physiological E2 module for the human anaphase-promoting complex
    • Williamson, A. et al. Identification of a physiological E2 module for the human anaphase-promoting complex. Proc. Natl Acad. Sci. USA 106, 18213-18218 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 18213-18218
    • Williamson, A.1
  • 28
    • 76549089605 scopus 로고    scopus 로고
    • UBE2S drives elongation of K11-linked ubiquitin chains by the anaphase-promoting complex
    • Wu, T. et al. UBE2S drives elongation of K11-linked ubiquitin chains by the anaphase-promoting complex. Proc. Natl Acad. Sci. USA 107, 1355-1360 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 1355-1360
    • Wu, T.1
  • 29
    • 77955516435 scopus 로고    scopus 로고
    • K11-linked polyubiquitination in cell cycle control revealed by a K11 linkage-specific antibody
    • Matsumoto, M. L. et al. K11-linked polyubiquitination in cell cycle control revealed by a K11 linkage-specific antibody. Mol. Cell 39, 477-484 (2010).
    • (2010) Mol. Cell , vol.39 , pp. 477-484
    • Matsumoto, M.L.1
  • 30
    • 84862776836 scopus 로고    scopus 로고
    • APC/C-mediated multiple monoubiquitylation provides an alternative degradation signal for cyclin B1
    • Dimova, N. V. et al. APC/C-mediated multiple monoubiquitylation provides an alternative degradation signal for cyclin B1. Nat. Cell Biol. 14, 168-176 (2012).
    • (2012) Nat. Cell Biol , vol.14 , pp. 168-176
    • Dimova, N.V.1
  • 31
    • 84880329682 scopus 로고    scopus 로고
    • Emi1 preferentially inhibits ubiquitin chain elongation by the anaphase-promoting complex
    • Wang, W. & Kirschner, M. W. Emi1 preferentially inhibits ubiquitin chain elongation by the anaphase-promoting complex. Nat. Cell Biol. 15, 797-806 (2013).
    • (2013) Nat. Cell Biol , vol.15 , pp. 797-806
    • Wang, W.1    Kirschner, M.W.2
  • 32
    • 80054750354 scopus 로고    scopus 로고
    • Processive ubiquitin chain formation by the anaphasepromoting complex
    • Meyer, H. J. & Rape, M. Processive ubiquitin chain formation by the anaphasepromoting complex. Semin. Cell Dev. Biol. 22, 544-550 (2011).
    • (2011) Semin. Cell Dev. Biol , vol.22 , pp. 544-550
    • Meyer, H.J.1    Rape, M.2
  • 34
    • 1642523634 scopus 로고    scopus 로고
    • Cell Cycle-Regulated Recognition of the Destruction Box of Cyclin B by the APC/C in Xenopus Egg Extracts
    • DOI 10.1016/S1097-2765(03)00480-5
    • Yamano, H., Gannon, J., Mahbubani, H. & Hunt, T. Cell cycle-regulated recognition of the destruction box of cyclin B by the APC/C in Xenopus egg extracts. Mol. Cell 13, 137-147 (2004). (Pubitemid 38117122)
    • (2004) Molecular Cell , vol.13 , Issue.1 , pp. 137-147
    • Yamano, H.1    Gannon, J.2    Mahbubani, H.3    Hunt, T.4
  • 35
    • 77957947338 scopus 로고    scopus 로고
    • Pharmacologic inhibition of the anaphase-promoting complex induces a spindle checkpoint-dependent mitotic arrest in the absence of spindle damage
    • Zeng, X. et al. Pharmacologic inhibition of the anaphase-promoting complex induces a spindle checkpoint-dependent mitotic arrest in the absence of spindle damage. Cancer Cell 18, 382-395 (2010).
    • (2010) Cancer Cell , vol.18 , pp. 382-395
    • Zeng, X.1
  • 36
    • 84858688402 scopus 로고    scopus 로고
    • An APC/C inhibitor stabilizes cyclin B1 by prematurely terminating ubiquitination
    • Zeng, X. & King, R. W. An APC/C inhibitor stabilizes cyclin B1 by prematurely terminating ubiquitination. Nat. Chem. Biol. 8, 383-392 (2012).
    • (2012) Nat. Chem. Biol , vol.8 , pp. 383-392
    • Zeng, X.1    King, R.W.2
  • 37
    • 34250799719 scopus 로고    scopus 로고
    • Cdc20: A WD40 Activator for a Cell Cycle Degradation Machine
    • DOI 10.1016/j.molcel.2007.06.009, PII S1097276507003759
    • Yu, H. Cdc20: a WD40 activator for a cell cycle degradation machine. Mol. Cell 27, 3-16 (2007). (Pubitemid 46991390)
    • (2007) Molecular Cell , vol.27 , Issue.1 , pp. 3-16
    • Yu, H.1
  • 38
    • 78650982520 scopus 로고    scopus 로고
    • Substrate binding on the APC/C occurs between the coactivator Cdh1 and the processivity factor Doc1
    • Buschhorn, B. A. et al. Substrate binding on the APC/C occurs between the coactivator Cdh1 and the processivity factor Doc1. Nat. Struct. Mol. Biol. 18, 6-13 (2011).
    • (2011) Nat. Struct. Mol. Biol , vol.18 , pp. 6-13
    • Buschhorn, B.A.1
  • 39
    • 79952290609 scopus 로고    scopus 로고
    • The mechanism of linkage-specific ubiquitin chain elongation by a single-subunit E2
    • Wickliffe, K. E., Lorenz, S., Wemmer, D. E., Kuriyan, J. & Rape, M. The mechanism of linkage-specific ubiquitin chain elongation by a single-subunit E2. Cell 144, 769-781 (2011).
    • (2011) Cell , vol.144 , pp. 769-781
    • Wickliffe, K.E.1    Lorenz, S.2    Wemmer, D.E.3    Kuriyan, J.4    Rape, M.5
  • 40
    • 0035370009 scopus 로고    scopus 로고
    • Emi1 is a mitotic regulator that interacts with Cdc20 and inhibits the anaphase promoting complex
    • DOI 10.1016/S0092-8674(01)00361-0
    • Reimann, J. D. R. et al. Emi1 is a mitotic regulator that interacts with Cdc20 and inhibits the anaphase promoting complex. Cell 105, 645-655 (2001). (Pubitemid 32524117)
    • (2001) Cell , vol.105 , Issue.5 , pp. 645-655
    • Reimann, J.D.R.1    Freed, E.2    Hsu, J.Y.3    Kramer, E.R.4    Peters, J.-M.5    Jackson, P.K.6
  • 41
    • 70450218366 scopus 로고    scopus 로고
    • Rapid E2-E3 assembly and disassembly enable processive ubiquitylation of cullin-RING ubiquitin ligase substrates
    • Kleiger, G., Saha, A., Lewis, S., Kuhlman, B. & Deshaies, R. J. Rapid E2-E3 assembly and disassembly enable processive ubiquitylation of cullin-RING ubiquitin ligase substrates. Cell 139, 957-968 (2009).
    • (2009) Cell , vol.139 , pp. 957-968
    • Kleiger, G.1    Saha, A.2    Lewis, S.3    Kuhlman, B.4    Deshaies, R.J.5
  • 42
    • 84880171038 scopus 로고    scopus 로고
    • Electron microscopy structure of human APC/CCDH1-EMI1 reveals multimodal mechanism of E3 ligase shutdown
    • Frye, J. J. et al. Electron microscopy structure of human APC/CCDH1-EMI1 reveals multimodal mechanism of E3 ligase shutdown. Nat. Struct. Mol. Biol. 20, 827-835 (2013).
    • (2013) Nat. Struct. Mol. Biol , vol.20 , pp. 827-835
    • Frye, J.J.1
  • 43
    • 79951491055 scopus 로고    scopus 로고
    • Structures of APC/CCdh1 with substrates identify Cdh1 and Apc10 as the D-box co-receptor
    • da Fonseca, P. C. A. et al. Structures of APC/CCdh1 with substrates identify Cdh1 and Apc10 as the D-box co-receptor. Nature 470, 274-278 (2011).
    • (2011) Nature , vol.470 , pp. 274-278
    • Da Fonseca, P.C.A.1
  • 45
    • 0036850233 scopus 로고    scopus 로고
    • The Doc1 subunit is a processivity factor for the anaphase-promoting complex
    • DOI 10.1038/ncb871
    • Carroll, C. W. & Morgan, D. O. The Doc1 subunit is a processivity factor for the anaphase-promoting complex. Nat. Cell Biol. 4, 880-887 (2002). (Pubitemid 35331363)
    • (2002) Nature Cell Biology , vol.4 , Issue.11 , pp. 880-887
    • Carroll, C.W.1    Morgan, D.O.2
  • 46
    • 11844279698 scopus 로고    scopus 로고
    • The APC subunit Doc1 promotes recognition of the substrate destruction box
    • DOI 10.1016/j.cub.2004.12.066, PII S0960982204010206
    • Carroll, C. W., Enquist-Newman, M. & Morgan, D. O. The APC subunit Doc1 promotes recognition of the substrate destruction box. Curr. Biol. 15, 11-18 (2005). (Pubitemid 40084696)
    • (2005) Current Biology , vol.15 , Issue.1 , pp. 11-18
    • Carroll, C.W.1    Enquist-Newman, M.2    Morgan, D.O.3
  • 47
    • 0037534899 scopus 로고    scopus 로고
    • βTrCP/Slimb ubiquitin ligase activates the anaphase promoting complex to allow progression beyond prometaphase
    • DOI 10.1016/S1534-5807(03)00153-9, PII S1534580703001539
    • Margottin-Goguet, F. et al. Prophase destruction of Emi1 by the SCFb-TrCP/ Slimb ubiquitin ligase activates the anaphase promoting complex to allow progression beyond prometaphase. Dev. Cell 4, 813-826 (2003). (Pubitemid 36676034)
    • (2003) Developmental Cell , vol.4 , Issue.6 , pp. 813-826
    • Margottin-Goguet, F.1    Hsu, J.Y.2    Loktev, A.3    Hsieh, H.-M.4    Reimann, J.D.R.5    Jackson, P.K.6
  • 49
    • 0034678923 scopus 로고    scopus 로고
    • Nek2B, a novel maternal form of Nek2 kinase, is essential for the assembly or maintenance of centrosomes in early Xenopus embryos
    • Uto, K. & Sagata, N. Nek2B, a novel maternal form of Nek2 kinase, is essential for the assembly or maintenance of centrosomes in early Xenopus embryos. EMBO J. 19, 1816-1826 (2000). (Pubitemid 30204393)
    • (2000) EMBO Journal , vol.19 , Issue.8 , pp. 1816-1826
    • Uto, K.1    Sagata, N.2
  • 50
    • 33846930369 scopus 로고    scopus 로고
    • Erp1/Emi2 is essential for the meiosis I to meiosis II transition in Xenopus oocytes
    • DOI 10.1016/j.ydbio.2006.10.044, PII S0012160606013388
    • Ohe, M., Inoue, D., Kanemori, Y. & Sagata, N. Erp1/Emi2 is essential for the meiosis I to meiosis II transition in Xenopus oocytes. Dev. Biol. 303, 157-164 (2007). (Pubitemid 46241095)
    • (2007) Developmental Biology , vol.303 , Issue.1 , pp. 157-164
    • Ohe, M.1    Inoue, D.2    Kanemori, Y.3    Sagata, N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.